Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.14.99.50: gamma-glutamyl hercynylcysteine S-oxide synthase

This is an abbreviated version!
For detailed information about gamma-glutamyl hercynylcysteine S-oxide synthase, go to the full flat file.

Word Map on EC 1.14.99.50

Reaction

hercynine
+
gamma-L-glutamyl-L-cysteine
 +
O2
=
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
 +
H2O

Synonyms

5-histidylcysteine sulfoxide synthase, Cabther_A1318, EgtB, EgtBthermo, hercynine oxygenase, sulfoxide synthase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.50 gamma-glutamyl hercynylcysteine S-oxide synthase

Crystallization

Crystallization on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.5 A resolution. Enzyme is a tetramer. The active site is located at the interface between the N- and C-terminal domains for each monomer where a mononuclear nonheme iron is coordinated by His62, His153, His157 and three water molecules in an octahedral arrangement
analysis of crystal structure of EgtB, PDB ID 4X8D, in complex with iron(II) and N-alpha-trimethylhistidine
analysis of the X-ray crystal structure of EgtB from Mycobacterium thermoresistibile, solved in three different forms, namely, the apo form, in complex with iron and the N-alpha-trimethyl histidine substrate, and in complex with manganese and the two natural substrates gamma-glutamyl cysteine and alpha-trimethyl histidine at 1.98 A resolution, with the active site for the third one. X-ray structure of the active site of EgtB complex with gamma-glutamyl cysteine and N-alpha-trimethyl histidine, coordinates taken from PDB ID 4X8D. Mn is replaced by Fe in the active site
purified recombinant enzyme, as iron-bound holoenzyme, in complex with substrate gamma-glutamyl cysteine, N-alpha-dimethyl histidine and Mn2+ or with substrate N-alpha-trimethyl histidine and Fe2+, X-ray diffraction structure determination and analysis